Biochemical properties of the high-molecular-weight glycopeptides released from the cell surface of human teratocarcinoma cells.
The present study deals with the biochemical properties of high-molecular-weight glycopeptides isolated from the surface of human teratocarcinoma cells. This cell surface material released by mild trypsin digestion from galactose-labeled human teratocarcinoma cells, Tera I and PA1, was digested extensively with pronase. Most of the resulting glycopeptides were large and were excluded from a Sephadex G-50 column. The properties of these large cell surface glycopeptides isolated from Tera I cells have been examined in detail. It is clear from these experiments that they are neither acidic mucopolysaccharides nor mucin-type glycopeptides with short oligosaccharide chains. Although the glycopeptides are hardly hydrolyzed by beta-galactosidase even after prior digestion with neuraminidase, around 30% of the glycopeptides are depolymerized by treatment with endo-beta-galactosidase from Escherichia freundii. The large cell surface glycopeptides from Tera I cells therefore appear to be very similar to the large glycopeptides seen on mouse embryonal carcinoma cells, which have core structures composed of galactose and N-acetylglucosamine. Like the mouse cell glycopeptides, a fraction of the large glycopeptides from these human cells bind to agarose-conjugated fucose-binding proteins and peanut agglutinin.
D000818:Animals; D001665:Binding Sites; D002460:Cell Line; D002462:Cell Membrane / Q000378:metabolism*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D006020:Glycopeptides / Q000302:isolation & purification* / Q000378:metabolism; D006801:Humans; D051379:Mice; D008970:Molecular Weight; D009439:Neuraminidase; D011402:Pronase; D013724:Teratoma / Q000378:metabolism*; D014357:Trypsin; D001616:beta-Galactosidase
D006020:Glycopeptides; D009439:Neuraminidase; D001616:beta-Galactosidase; D014357:Trypsin; D011402:Pronase